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dc:description: MIF Leishmania homologues adopt extended ?-helix H1. (A) Superimposition of wt human and Leishmania MIF monomers. Note the extension of the helix H1 in the Leishmania species, in comparison to the crystal structure of the human protein. (B) Multiple sequence alignment of wt huMIF and the two species of Leishmania MIF. Residues highlighted in squares correspond to the hydrophobic pocket, while residues underlined correspond to the tautomerase enzymatic site.(TIFF)
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description: MIF Leishmania homologues adopt extended ?-helix H1. (A) Superimposition of wt human and Leishmania MIF monomers. Note the extension of the helix H1 in the Leishmania species, in comparison to the crystal structure of the human protein. (B) Multiple sequence alignment of wt huMIF and the two species of Leishmania MIF. Residues highlighted in squares correspond to the hydrophobic pocket, while residues underlined correspond to the tautomerase enzymatic site.(TIFF)
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title: Figure S5
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dc:title: Figure S5
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